NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|966923762|ref|XP_014980751|]
View 

myelin protein zero-like protein 1 isoform X2 [Macaca mulatta]

Protein Classification

Ig_P0-like domain-containing protein( domain architecture ID 10146023)

Ig_P0-like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
38-154 3.11e-70

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


:

Pssm-ID: 409380  Cd Length: 117  Bit Score: 209.59  E-value: 3.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  38 LEVYTPKEIFVANGTQGKLTCKFKSTDETGGLTSVTWSFQPEGADTTVSFFHYSQGQVYPGNYPPFKDRISWAGDLDKKD 117
Cdd:cd05715    1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966923762 118 ASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYV 154
Cdd:cd05715   81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
 
Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
38-154 3.11e-70

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 209.59  E-value: 3.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  38 LEVYTPKEIFVANGTQGKLTCKFKSTDETGGLTSVTWSFQPEGADTTVSFFHYSQGQVYPGNYPPFKDRISWAGDLDKKD 117
Cdd:cd05715    1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966923762 118 ASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYV 154
Cdd:cd05715   81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
41-155 3.84e-26

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 97.14  E-value: 3.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762   41 YTPKEIFVANGTQGKLTCKFKSTdETGGLTSVTWSFQPEGADTTVSFFHYSQGQvypgNYPPFKDRISWAGDLDKKDASI 120
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYSNGS----EEGVKKGRFSGRGDPSNGDGSL 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 966923762  121 NIENMQFIHNGTYICDVkNPPDIVVQPGHIRLYVV 155
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
55-137 3.87e-11

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 57.01  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762    55 KLTCKFKSTDETGglTSVTWSFQPEGADTTVSFFHYSQGQVYPGNYppFKDRISWAGDLDKKDASINIENMQFIHNGTYI 134
Cdd:smart00406   3 TLSCKFSGSTFSS--YYVSWVRQPPGKGLEWLGYIGSNGSSYYQES--YKGRFTISKDTSKNDVSLTISNLRVEDTGTYY 78

                   ...
gi 966923762   135 CDV 137
Cdd:smart00406  79 CAV 81
 
Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
38-154 3.11e-70

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 209.59  E-value: 3.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  38 LEVYTPKEIFVANGTQGKLTCKFKSTDETGGLTSVTWSFQPEGADTTVSFFHYSQGQVYPGNYPPFKDRISWAGDLDKKD 117
Cdd:cd05715    1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966923762 118 ASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYV 154
Cdd:cd05715   81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
38-154 2.16e-39

Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 131.15  E-value: 2.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  38 LEVYTPKEIFVANGTQGKLTCKFKSTDETGGLTSVTWSFQPEGADTTVSFFHYSQGQVYPGNYPPFKDRISWAGDLDKKD 117
Cdd:cd05879    1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966923762 118 ASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYV 154
Cdd:cd05879   81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
38-154 3.94e-35

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 120.32  E-value: 3.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  38 LEVYTPKEIFVANGTQGKLTCKFKSTDETGGLTSVTWSFQPEGADTTVSFFHYSQgQVYPGNYPPFKDRISWAGDLDKKD 117
Cdd:cd05880    1 IEVYTSKEVEAVNGTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHK-RPYPPPDGRFKGRVVWDGNIMRRD 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966923762 118 ASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYV 154
Cdd:cd05880   80 ASILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV 116
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
41-155 3.84e-26

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 97.14  E-value: 3.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762   41 YTPKEIFVANGTQGKLTCKFKSTdETGGLTSVTWSFQPEGADTTVSFFHYSQGQvypgNYPPFKDRISWAGDLDKKDASI 120
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYSNGS----EEGVKKGRFSGRGDPSNGDGSL 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 966923762  121 NIENMQFIHNGTYICDVkNPPDIVVQPGHIRLYVV 155
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTVL 109
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
45-152 1.91e-14

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 66.71  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  45 EIFVANGTQGKLTCKFKSTDETGGLTSVTWSFQP-EGADTTVsfFHYSQGQVYPGNYPPFKDRISWAGDLDKKDASINIE 123
Cdd:cd20960    9 EIKKVAGENVTLPCHHQLGLEDQGTLDIEWLLLPsDKVEKVV--ITYSGDRVYNHYYPALKGRVAFTSNDLSGDASLNIS 86
                         90       100
                 ....*....|....*....|....*....
gi 966923762 124 NMQFIHNGTYICDVKNPPDivVQPGHIRL 152
Cdd:cd20960   87 NLKLSDTGTYQCKVKKAPG--YAWSKITL 113
IGv smart00406
Immunoglobulin V-Type;
55-137 3.87e-11

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 57.01  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762    55 KLTCKFKSTDETGglTSVTWSFQPEGADTTVSFFHYSQGQVYPGNYppFKDRISWAGDLDKKDASINIENMQFIHNGTYI 134
Cdd:smart00406   3 TLSCKFSGSTFSS--YYVSWVRQPPGKGLEWLGYIGSNGSSYYQES--YKGRFTISKDTSKNDVSLTISNLRVEDTGTYY 78

                   ...
gi 966923762   135 CDV 137
Cdd:smart00406  79 CAV 81
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
51-137 1.55e-06

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 45.52  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  51 GTQGKLTCKFKSTdETGGLTSVTWSFQPEGADTTVSFFHYSQGQVYPGnypPFKDRISW-AGDLDKKDASINIENMQFIH 129
Cdd:cd05718   14 GGSVTLPCSLTSP-GTTKITQVTWMKIGAGSSQNVAVFHPQYGPSVPN---PYAERVEFlAARLGLRNATLRIRNLRVED 89

                 ....*...
gi 966923762 130 NGTYICDV 137
Cdd:cd05718   90 EGNYICEF 97
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
51-139 2.12e-04

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 39.50  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  51 GTQGKLTCKFKSTDETGGLTsVTWsfQPEGADTTVSFFHYSQGQVYPGNyPPFKDRIS-WAGDLDKKDASINIENMQFIH 129
Cdd:cd20984   12 GEDGILSCTFTPDIKLSDIV-IQW--LKEGDSGLVHEFKEGKDELSRQS-PMFRGRTSlFADQVHVGNASLRLKNVQLTD 87
                         90
                 ....*....|
gi 966923762 130 NGTYICDVKN 139
Cdd:cd20984   88 AGTYLCIISN 97
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
51-141 4.35e-04

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 409469  Cd Length: 113  Bit Score: 38.41  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762  51 GTQGKLTCKFKSTDETGGLTSVTWSFQPEGADTTVSFFHYSQGQVYpgnYPPFKDRISWAGDlDKKDASINIENMQFIHN 130
Cdd:cd05886   14 GTDVVLHCSFANPLPSVKITQVTWQKSTNGSKQNVAIYNPSMGVSV---LPPYRERVTFLNP-SFTDGTIRLSRLELEDE 89
                         90
                 ....*....|.
gi 966923762 131 GTYICDVKNPP 141
Cdd:cd05886   90 GVYICEFATFP 100
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
43-154 4.67e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 35.17  E-value: 4.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923762    43 PKEIFVANGTQGKLTCKFKSTDETggltSVTWSFQPegadttvsffhysqgqvypGNYPPFKDRISWagDLDKKDASINI 122
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPP----EVTWYKQG-------------------GKLLAESGRFSV--SRSGSTSTLTI 55
                           90       100       110
                   ....*....|....*....|....*....|..
gi 966923762   123 ENMQFIHNGTYICDVKNPPDIVVqpGHIRLYV 154
Cdd:smart00410  56 SNVTPEDSGTYTCAATNSSGSAS--SGTTLTV 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH